2Y0N
CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN DOSAGE COMPENSATION FACTORS MSL1 AND MSL3
2Y0N の概要
| エントリーDOI | 10.2210/pdb2y0n/pdb |
| 分子名称 | MALE-SPECIFIC LETHAL 3 HOMOLOG, MALE-SPECIFIC LETHAL 1 HOMOLOG (2 entities in total) |
| 機能のキーワード | transcription, chromatin, x chromosome, msl complex |
| 由来する生物種 | HOMO SAPIENS (HUMAN) 詳細 |
| 細胞内の位置 | Nucleus (Probable): Q8N5Y2 Nucleus: Q6PDM1 |
| タンパク質・核酸の鎖数 | 8 |
| 化学式量合計 | 124190.98 |
| 構造登録者 | Kadlec, J.,Hallacli, E.,Lipp, M.,Holz, H.,Sanchez Weatherby, J.,Cusack, S.,Akhtar, A. (登録日: 2010-12-04, 公開日: 2011-01-12, 最終更新日: 2023-12-20) |
| 主引用文献 | Kadlec, J.,Hallacli, E.,Lipp, M.,Holz, H.,Sanchez-Weatherby, J.,Cusack, S.,Akhtar, A. Structural Basis for Mof and Msl3 Recruitment Into the Dosage Compensation Complex by Msl1. Nat.Struct.Mol.Biol., 18:142-, 2011 Cited by PubMed Abstract: The male-specific lethal (MSL) complex is required for dosage compensation in Drosophila melanogaster, and analogous complexes exist in mammals. We report structures of binary complexes of mammalian MSL3 and the histone acetyltransferase (HAT) MOF with consecutive segments of MSL1. MSL1 interacts with MSL3 as an extended chain forming an extensive hydrophobic interface, whereas the MSL1-MOF interface involves electrostatic interactions between the HAT domain and a long helix of MSL1. This structure provides insights into the catalytic mechanism of MOF and enables us to show analogous interactions of MOF with NSL1. In Drosophila, selective disruption of Msl1 interactions with Msl3 or Mof severely affects Msl1 targeting to the body of dosage-compensated genes and several high-affinity sites, without affecting promoter binding. We propose that Msl1 acts as a scaffold for MSL complex assembly to achieve specific targeting to the X chromosome. PubMed: 21217699DOI: 10.1038/NSMB.1960 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (3 Å) |
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